REGE1_CAEEL
ID REGE1_CAEEL Reviewed; 634 AA.
AC Q95YE2; G4S4L8;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 5.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Endoribonuclease rege-1 {ECO:0000305|PubMed:27746047};
DE EC=3.1.-.- {ECO:0000269|PubMed:27746047};
DE AltName: Full=Zinc finger CCCH domain-containing protein rege-1 {ECO:0000305};
GN Name=rege-1 {ECO:0000303|PubMed:27746047, ECO:0000312|WormBase:C30F12.1};
GN ORFNames=C30F12.1 {ECO:0000312|WormBase:C30F12.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18425118; DOI=10.1038/ncb1718;
RA Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
RA Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
RT "A pathway for phagosome maturation during engulfment of apoptotic cells.";
RL Nat. Cell Biol. 10:556-566(2008).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-231; ASP-313; ASP-314 AND
RP ASP-332.
RX PubMed=27746047; DOI=10.1016/j.devcel.2016.09.018;
RA Habacher C., Guo Y., Venz R., Kumari P., Neagu A., Gaidatzis D.,
RA Harvald E.B., Faergeman N.J., Gut H., Ciosk R.;
RT "Ribonuclease-mediated control of body fat.";
RL Dev. Cell 39:359-369(2016).
CC -!- FUNCTION: Endonuclease which binds to the 3'UTR of target mRNAs and
CC induces degradation of the transcript (PubMed:27746047). Negatively
CC regulates the expression of the transcription factor ets-4, which
CC probably controls the expression of lipid metabolism genes
CC (PubMed:27746047). May play a role in the clearance of apoptotic cell
CC corpses (PubMed:18425118). {ECO:0000269|PubMed:18425118,
CC ECO:0000269|PubMed:27746047}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q5D1E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:27746047}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestinal cells adjacent to the
CC pharynx. {ECO:0000269|PubMed:27746047}.
CC -!- DISRUPTION PHENOTYPE: Viable, but exhibit slower development and have
CC reduced body fat (PubMed:27746047). RNAi-mediated knockdown results in
CC increased sensitivity and reduced survival in response to lower
CC temperatures (PubMed:27746047). RNAi-mediated knockdown results in
CC increased expression of the transcription factor ets-4 in the nuclei of
CC intestinal cells, which may further result in changes in the expression
CC of genes involved in lipid metabolism (PubMed:27746047). RNAi-mediated
CC knockdown also causes a defect in the clearance of apoptotic cell
CC corpses in hermaphrodite gonads (PubMed:18425118).
CC {ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:27746047}.
CC -!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
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DR EMBL; BX284601; CCD66238.1; -; Genomic_DNA.
DR RefSeq; NP_491985.4; NM_059584.5.
DR AlphaFoldDB; Q95YE2; -.
DR SMR; Q95YE2; -.
DR DIP; DIP-25963N; -.
DR IntAct; Q95YE2; 1.
DR STRING; 6239.C30F12.1; -.
DR EPD; Q95YE2; -.
DR PaxDb; Q95YE2; -.
DR PeptideAtlas; Q95YE2; -.
DR EnsemblMetazoa; C30F12.1.1; C30F12.1.1; WBGene00016260.
DR GeneID; 172426; -.
DR KEGG; cel:CELE_C30F12.1; -.
DR UCSC; C30F12.1; c. elegans.
DR CTD; 172426; -.
DR WormBase; C30F12.1; CE40689; WBGene00016260; rege-1.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000170648; -.
DR HOGENOM; CLU_013020_2_0_1; -.
DR InParanoid; Q95YE2; -.
DR OMA; ERANGQH; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; Q95YE2; -.
DR PRO; PR:Q95YE2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00016260; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR InterPro; IPR040546; Rege-1_UBA-like.
DR InterPro; IPR040757; Regnase_1/ZC3H12_C.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF18561; Regnase_1_C; 1.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
DR Pfam; PF18039; UBA_6; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..634
FT /note="Endoribonuclease rege-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438851"
FT DOMAIN 225..377
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT ZN_FING 387..412
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT MUTAGEN 231
FT /note="D->N: Loss of ribonuclease activity; when associated
FT with A-313, A-314 and A-332."
FT /evidence="ECO:0000269|PubMed:27746047"
FT MUTAGEN 313
FT /note="D->A: Loss of ribonuclease activity; when associated
FT with N-231; A-314 and A-332."
FT /evidence="ECO:0000269|PubMed:27746047"
FT MUTAGEN 314
FT /note="D->A: Loss of ribonuclease activity; when associated
FT with N-231; A-313, and A-332."
FT /evidence="ECO:0000269|PubMed:27746047"
FT MUTAGEN 332
FT /note="D->A: Loss of ribonuclease activity; when associated
FT with N-231; A-313 and A-314."
FT /evidence="ECO:0000269|PubMed:27746047"
SQ SEQUENCE 634 AA; 70582 MW; CCAF5C3B145186BC CRC64;
MDSTARGHAP LCRTSNQRGL GTRLNPYYQS TPHQPMVQSM SNPIGSYGEQ GNAQIIGSSG
QVLSTGPPPG LAPVQCNDFD SCYSSCDDIS HPSLSRESSD PSKIDDDQTA PMIRYPAPEV
VEFATKLGYS TEQLSHVLNT IGVDSRMDDV LSELVKMGLP GGKPENSGKS GSRNSPEPIM
TSSASSSSAS SSSSHRPIRQ SVSIATSSPA TSSSTPSKYN PDPSLRAVVV DGSNVAMLHG
RKEVFSCAGL RECLNYFLER GHPEVLIFIP QYRREQPRSD SPITDQHILQ EIERHIIYTP
SRNVNGRRVV CHDDRYILRT AELKDAVIVS NDEYRDLTRE NPAWRKIVEE RLLMFTFVED
KFMPPDDPSG RHGPRIESFL SKVPVVSSNP LVCPYARKCT YGNKCKFYHP ERANGQHMSV
TERLMKENQQ KKSLGAVKSM QYEMFKNKHA ALSRTQSLNV VKQLTENMSQ LPPTPESPMQ
MPRQHMQLQQ ANSAPWQQHT VVQRHGSSPL TPVNRQMNVY PDMYNMSQQQ NHQVLPNQHG
VIGGQRPPKM TTTVSQTHLF APSTAVWGHS ELSVGPVNTG SDESLAEVRS RVHFHLCNIF
PHDFVESVMA ANPEEVNAPV LCELIIRAQK EYRK
